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1ve7

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(New page: 200px<br /><applet load="1ve7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ve7, resolution 2.7&Aring;" /> '''Crystal structure of ...)
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[[Image:1ve7.gif|left|200px]]<br /><applet load="1ve7" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1ve7, resolution 2.7&Aring;" />
 
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'''Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate'''<br />
 
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==Overview==
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==Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate==
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Acylpeptide hydrolases (APH; also known as acylamino acid releasing, enzyme) catalyze the removal of an N-acylated amino acid from blocked, peptides. The crystal structure of an APH from the thermophilic archaeon, Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the, prolyl oligopeptidase family of serine proteases. The structure of apAPH, is a symmetric homodimer with each subunit comprised of two domains. The, N-terminal domain is a regular seven-bladed beta-propeller, while the, C-terminal domain has a canonical alpha/beta hydrolase fold and includes, the active site and a conserved Ser445-Asp524-His556 catalytic triad. The, complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure, unambiguously maps out the substrate binding pocket and provides a basis, for substrate recognition by apAPH. A conserved mechanism for protein, degradation from archaea to mammals is suggested by the structural, features of apAPH.
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<StructureSection load='1ve7' size='340' side='right'caption='[[1ve7]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1ve7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VE7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1VE7 FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.7&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4NP:4-NITROPHENYL+PHOSPHATE'>4NP</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ve7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ve7 OCA], [https://pdbe.org/1ve7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ve7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ve7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ve7 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/APEH_AERPE APEH_AERPE] This enzyme catalyzes the hydrolysis of the N-terminal peptide bond of an N-acetylated peptide to generate an N-acetylated amino acid and a peptide with a free N-terminus.
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ve/1ve7_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ve7 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Acylpeptide hydrolases (APH; also known as acylamino acid releasing enzyme) catalyze the removal of an N-acylated amino acid from blocked peptides. The crystal structure of an APH from the thermophilic archaeon Aeropyrum pernix K1 to 2.1 A resolution confirms it to be a member of the prolyl oligopeptidase family of serine proteases. The structure of apAPH is a symmetric homodimer with each subunit comprised of two domains. The N-terminal domain is a regular seven-bladed beta-propeller, while the C-terminal domain has a canonical alpha/beta hydrolase fold and includes the active site and a conserved Ser445-Asp524-His556 catalytic triad. The complex structure of apAPH with an organophosphorus substrate, p-nitrophenyl phosphate, has also been determined. The complex structure unambiguously maps out the substrate binding pocket and provides a basis for substrate recognition by apAPH. A conserved mechanism for protein degradation from archaea to mammals is suggested by the structural features of apAPH.
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==About this Structure==
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Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1.,Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z Structure. 2004 Aug;12(8):1481-8. PMID:15296741<ref>PMID:15296741</ref>
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1VE7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Aeropyrum_pernix Aeropyrum pernix] with 4NP and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Acylaminoacyl-peptidase Acylaminoacyl-peptidase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.19.1 3.4.19.1] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1VE7 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1., Bartlam M, Wang G, Yang H, Gao R, Zhao X, Xie G, Cao S, Feng Y, Rao Z, Structure. 2004 Aug;12(8):1481-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15296741 15296741]
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</div>
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[[Category: Acylaminoacyl-peptidase]]
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<div class="pdbe-citations 1ve7" style="background-color:#fffaf0;"></div>
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[[Category: Aeropyrum pernix]]
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[[Category: Single protein]]
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[[Category: Bartlam, M.]]
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[[Category: Cao, S.]]
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[[Category: Feng, Y.]]
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[[Category: Gao, R.]]
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[[Category: Rao, Z.]]
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[[Category: Wang, G.]]
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[[Category: Xie, G.]]
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[[Category: Yang, H.]]
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[[Category: Zhao, X.]]
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[[Category: 4NP]]
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[[Category: GOL]]
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[[Category: alpha/beta hydrolase domain]]
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[[Category: beta propeller domain]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 04:46:09 2007''
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==See Also==
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*[[Acylaminoacyl peptidase 3D structures|Acylaminoacyl peptidase 3D structures]]
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Aeropyrum pernix]]
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[[Category: Large Structures]]
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[[Category: Bartlam M]]
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[[Category: Cao S]]
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[[Category: Feng Y]]
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[[Category: Gao R]]
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[[Category: Rao Z]]
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[[Category: Wang G]]
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[[Category: Xie G]]
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[[Category: Yang H]]
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[[Category: Zhao X]]

Current revision

Crystal structure of an acylpeptide hydrolase/esterase from Aeropyrum pernix K1 in complex with p-nitrophenyl phosphate

PDB ID 1ve7

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